Ligand-dependent intra- and inter-domain motions in the PDZ12 tandem regulate binding interfaces in postsynaptic density protein-95.

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ID: 54605
2019
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Abstract
The postsynaptic density protein-95 (PSD-95) regulates synaptic plasticity through interactions mediated by its peptide binding PDZ domains. The two N-terminal PDZ domains of PSD-95 form an autonomous structural unit, and their interdomain orientation and dynamics depend on ligand binding. To understand the mechanistic details of the effect of ligand binding, we generated conformational ensembles using available experimentally determined NOE interatomic distances and S order parameters. In our approach, the fast dynamics of the two domains is treated independently. We find that intradomain structural changes induced by ligand binding modulate the probability of the occurrence of specific domain-domain orientations. Our results suggest that the β2-β3 loop in the PDZ domains is a key regulatory region, which influences both intradomain motions and supramodular rearrangement.
Reference Key
kovcs2019liganddependentfebs Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Kovács, Bertalan;Zajácz-Epresi, Nóra;Gáspári, Zoltán;
Journal FEBS Letters
Year 2019
DOI
10.1002/1873-3468.13626
URL
Keywords
molecular dynamics simulation pdz tandem psd-95 structural ensembles supramodular dynamics

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